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Erythrocyte membrane protein band 4.2

P4.2, erythrocyte protein 4.2, EPB42, erythrocyte membrane protein band 4.2, Epb4.2
Erythrocyte membrane protein band 4.2 is an ATP-binding protein which may regulate the association of protein 3 with ankyrin. It probably has a role in erythrocyte shape and mechanical property regulation. Mutations in the EPB42 gene are associated with recessive spherocytic elliptocytosis and recessively transmitted hereditary hemolytic anemia. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, HS-2, Transglutaminase, HPP, HAD
Papers on P4.2
EPB42-Related Hereditary Spherocytosis
Begtrup et al., Seattle, United States. In Unknown Journal, 13 Apr 2014
DISEASE CHARACTERISTICS: EPB42-related hereditary spherocytosis (EPB42-HS) is a chronic non-immune hemolytic anemia that is usually of mild to moderate severity.
3-Deazaneplanocin A (DZNep), an inhibitor of S-adenosyl-methionine-dependent methyltransferase, promotes erythroid differentiation.
Harigae et al., Japan. In J Biol Chem, 03 Mar 2014
Transcriptional profiling of DZNep-treated K562 cells revealed marked upregulation of SLC4A1 and EPB42, previously reported as representative targets of the transcriptional corepressor ETO2.
Variations in both α-spectrin (SPTA1) and β-spectrin ( SPTB ) in a neonate with prolonged jaundice in a family where nine individuals had hereditary elliptocytosis.
Yaish et al., Salt Lake City, United States. In Neonatology, Dec 2013
No mutations were identified in ANK1 (ankyrin-1), SLC4A1 (band 3), EPB41 (band 4.1), or EPB42 (band 4.2).
Acute kernicterus in a neonate with O/B blood group incompatibility and a mutation in SLC4A1.
Prchal et al., Salt Lake City, United States. In Pediatrics, Aug 2013
No mutations were identified in other red cell cytoskeleton genes (ANK1, SPTA1, SPTB, EPB41, EPB42) and the UGT1A1 promoter region was normal.
Expression of different forms of transglutaminases by immature cells of Helianthus tuberosus sprout apices.
Del Duca et al., Roma, Italy. In Amino Acids, 2013
The composition of the two larger bands presented great similarities with annotated TGs; in particular, the 75 kDa form was very similar to mammalian inactive EPB42.
Protein 4.2 interaction with hereditary spherocytosis mutants of the cytoplasmic domain of human anion exchanger 1.
Reithmeier et al., Toronto, Canada. In Biochem J, 2011
study shows that cytoplasmic hereditary spherocytosis mutants cause impaired binding of protein 4.2 to AE1, leaving protein 4.2 susceptible to loss during erythrocyte development
Investigating the key membrane protein changes during in vitro erythropoiesis of protein 4.2 (-) cells (mutations Chartres 1 and 2).
Toye et al., Bristol, United Kingdom. In Haematologica, 2010
BACKGROUND: Protein 4.2 deficiency caused by mutations in the EPB42 gene results in hereditary spherocytosis with characteristic alterations of CD47, CD44 and RhAG.
Splenectomy and partial splenectomy improve hematopoietic stem cell engraftment in hypersplenic mice.
Rice et al., Durham, United States. In J Pediatr Surg, 2010
METHODS: We performed total splenectomy (n = 22), partial splenectomy (n = 16), or sham laparotomy (n = 21) on erythrocyte protein 4.2 knockout mice, a murine model of hereditary spherocytosis with hypersplenism.
Protein 4.2 binds to the carboxyl-terminal EF-hands of erythroid alpha-spectrin in a calcium- and calmodulin-dependent manner.
Lux et al., Boston, United States. In J Biol Chem, 2010
Data suggest that one or both of proteins 4.1 and 4.2 cause a portion of band 3 to localize near the spectrin-actin junctions and provide another point of attachment between the membrane skeleton and the lipid bilayer.
The use of real-time PCR technique in the detection of novel protein 4.2 gene mutations that coexist with thalassaemia alpha in a single patient.
Burzynska et al., Warsaw, Poland. In Eur J Haematol, 2009
mRNA relative quantification of red cell membrane protein genes in a Polish patient with alpha-thalassaemia trait indicated EPB42 as the gene that could also be involved in anaemia pathogenesis.
LSD1-mediated epigenetic modification is required for TAL1 function and hematopoiesis.
Huang et al., Gainesville, United States. In Proc Natl Acad Sci U S A, 2009
Consistent with the rapid changes of TAL1-corepressor complex during differentiation, TAL1 recruits LSD1 to the silenced p4.2 promoter in undifferentiated, but not in differentiated, murine erythroleukemia (MEL) cells.
Protein 4.2: a complex linker.
Toye et al., Bristol, United Kingdom. In Blood Cells Mol Dis, 2009
Current understanding of protein 4.2, its known interactions & implications of protein 4.2 deficiency are reviewed. A new speculative "open" homology structure for the the active, membrane associated form is proposed. Review.
Palm-based standard reference materials for iodine value and slip melting point.
Kuntom et al., Kuala Selangor, Malaysia. In Anal Chem Insights, 2007
The iodine value and slip melting point of palm oil, palm olein and palm stearin were determined in accordance to MPOB Test Methods p3.2:2004 and p4.2:2004, respectively.
Associations of protein 4.2 with band 3 and ankyrin.
Zhang et al., Shanghai, China. In Mol Cell Biochem, 2006
The interactions of three protein 4.2-derived recombinant proteins with CDB3 and ankyrin were investigated by using Far-Western blot and pull-down assay.
[Molecular mechanism of hereditary spherocytosis].
Sikorski et al., Laizhou, China. In Pol Merkur Lekarski, 2006
Hereditary spherocytosis stems from mutations in one of the genes encoding ankyrin-1 (ANKI), alpha spectrin (SPTA1) and beta spectrin (SPTB), the anion exchanger 1 (SLC4A 1), and protein 4.2 (EPB42).
Akt phosphorylates Tal1 oncoprotein and inhibits its repressor activity.
Pekarsky et al., Columbus, United States. In Cancer Res, 2005
Using luciferase assay, we showed that phosphorylation of Tal1 by Akt decreased repressor activity of Tal1 on EpB42 (P4.2) promoter.
Identification of a TAL1 target gene reveals a positive role for the LIM domain-binding protein Ldb1 in erythroid gene expression and differentiation.
Brandt et al., Nashville, United States. In Mol Cell Biol, 2003
Data show that a nuclear complex containing TAL1 and LIM domain-binding protein Ldb1 transactivates the protein 4.2 (P4.2) gene
Red blood cell membrane defects.
Stewart et al., Foggia, Italy. In Rev Clin Exp Hematol, 2003
The mutations of most cases of HS are located in the following genes: ANK1, SPTB, SLC4A1, EPB42 and SPTA1, which encode for ankyrin, spectrin beta-chain, the anion exchanger 1 (band 3), protein 4.2 and spectrin alpha-chain, respectively.
Molecular basis of red cell membrane disorders.
Delaunay, Le Kremlin-Bicêtre, France. In Acta Haematol, 2001
The mutations of most cases of hereditary spherocytosis (HS) are located in the following genes: ANK1, SPTB, SLC4A1, EPB42 and SPTA1, which encode ankyrin, spectrin beta-chain, the anion exchanger 1 (band 3), protein 4.2 and spectrin alpha-chain, respectively.
The murine pallid mutation is a platelet storage pool disease associated with the protein 4.2 (pallidin) gene.
Lux et al., Boston, United States. In Nat Genet, 1992
We have mapped the murine gene for protein 4.2 (Epb4.2) to chromosome 2 where it co-localizes with pallid.
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